Immunolocalisation of spermidine synthase in Solanum tuberosum

Spermidine synthase (SPDS) catalyses the formation of spermidine, which is an essential polyamine and widespread in living organisms. Spermidine is formed from putrescine by transfer of an aminopropyl group from decarboxylated S-adenosylmethionine. Spermidine is also a precursor to further polyamines, such as spermine and thermospermine, most of which contribute to tolerance against drought and salinity in plants. Thermospermine is indispensible for vascular tissue growth. Plant spermidine synthases have been cloned from several angiosperms; organ-specific gene expression levels are known for Arabidopsis only. In this study, immunolocalisation of SPDS in potato (Solanum tuberosum) organs is presented. Polyclonal antibodies for SPDS from potato produced in rabbits were purified by affinity chromatography. Cross-reaction with potato putrescine N-methyltransferase was eliminated. Accumulation of SPDS protein in the phloem region of vascular tissues throughout the potato plant is demonstrated.